Purification and partial characterization of a bovine epidermal growth factor-like polupeptide

J. C. Byatt; B. R. Larson; M. P. Baganoff; M. F. McGrath; R. J. Collier

Purification and partial characterization of a bovine epidermal growth factor-like polupeptide

J. C. Byatt, B. R. Larson, M. P. Baganoff, M. F. McGrath, R. J. Collier

Research output: Contribution to journal › Article › peer-review

Abstract

A heterologous radioreceptor assay was developed to follow the purification of an EGF-like polypeptide from bovine kidney. Purification of the growth factor was facilitated by the use of a novel affinity column using fixed A431 cells attached to sephadex beads. The mol. wt. of the purified EGF-LP was estimated to be 5480 from the amino acid composition. The purified EGF-like polypeptide stimulated the proliferation of bovine mammary epithelial cells and appeared to be equipotent to mouse EGF. Available evidence suggests that the purified molecule is distinct from bovine TGF-alpha.

Original language	English (US)
Pages (from-to)	1179-1187
Number of pages	9
Journal	Biochemistry International
Volume	20
Issue number	6
State	Published - 1990
Externally published	Yes

ASJC Scopus subject areas

Biochemistry

Cite this

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title = "Purification and partial characterization of a bovine epidermal growth factor-like polupeptide",

abstract = "A heterologous radioreceptor assay was developed to follow the purification of an EGF-like polypeptide from bovine kidney. Purification of the growth factor was facilitated by the use of a novel affinity column using fixed A431 cells attached to sephadex beads. The mol. wt. of the purified EGF-LP was estimated to be 5480 from the amino acid composition. The purified EGF-like polypeptide stimulated the proliferation of bovine mammary epithelial cells and appeared to be equipotent to mouse EGF. Available evidence suggests that the purified molecule is distinct from bovine TGF-alpha.",

author = "Byatt, {J. C.} and Larson, {B. R.} and Baganoff, {M. P.} and McGrath, {M. F.} and Collier, {R. J.}",

year = "1990",

language = "English (US)",

volume = "20",

pages = "1179--1187",

journal = "Biochemistry and Molecular Biology International",

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T1 - Purification and partial characterization of a bovine epidermal growth factor-like polupeptide

AU - Byatt, J. C.

AU - Larson, B. R.

AU - Baganoff, M. P.

AU - McGrath, M. F.

AU - Collier, R. J.

PY - 1990

Y1 - 1990

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AB - A heterologous radioreceptor assay was developed to follow the purification of an EGF-like polypeptide from bovine kidney. Purification of the growth factor was facilitated by the use of a novel affinity column using fixed A431 cells attached to sephadex beads. The mol. wt. of the purified EGF-LP was estimated to be 5480 from the amino acid composition. The purified EGF-like polypeptide stimulated the proliferation of bovine mammary epithelial cells and appeared to be equipotent to mouse EGF. Available evidence suggests that the purified molecule is distinct from bovine TGF-alpha.

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AN - SCOPUS:0025293023

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JO - Biochemistry and Molecular Biology International

JF - Biochemistry and Molecular Biology International

IS - 6

ER -

Purification and partial characterization of a bovine epidermal growth factor-like polupeptide

Abstract

ASJC Scopus subject areas

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